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Protein

Probable formate dehydrogenase

Gene

aciA

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

Formate + NAD+ = CO2 + NADH.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei259 – 2591By similarity
Binding sitei283 – 2831NADBy similarity
Active sitei312 – 3121Proton donorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi175 – 1762NADBy similarity
Nucleotide bindingi257 – 2593NADBy similarity
Nucleotide bindingi312 – 3154NADBy similarity

GO - Molecular functioni

  1. formate dehydrogenase (NAD+) activity Source: UniProtKB-EC
  2. NAD binding Source: InterPro
  3. oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Source: InterPro

GO - Biological processi

  1. acetate metabolic process Source: ASPGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Probable formate dehydrogenase (EC:1.2.1.2)
Alternative name(s):
NAD-dependent formate dehydrogenase
Short name:
FDH
Gene namesi
Name:aciA
ORF Names:AN6525
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560 Componenti: Chromosome I

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: ASPGD
  2. intracellular Source: ASPGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 365365Probable formate dehydrogenasePRO_0000076024Add
BLAST

Proteomic databases

PRIDEiQ03134.

Expressioni

Inductioni

Acetate induction mediated by amda regulatory gene.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi162425.CADANIAP00007297.

Structurei

3D structure databases

ProteinModelPortaliQ03134.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1052.
HOGENOMiHOG000136703.
InParanoidiQ03134.
KOiK00122.
OMAiGCRRVEN.
OrthoDBiEOG769ZV3.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiIPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR029753. D-isomer_DH_CS.
IPR029752. D-isomer_DH_CS1.
IPR006140. D-isomer_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view]
PROSITEiPS00065. D_2_HYDROXYACID_DH_1. 1 hit.
PS00670. D_2_HYDROXYACID_DH_2. 1 hit.
PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q03134-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKVLMVLYD GGSHAKDQPG LLGTTENELG IRKWIEEQGH TLVTTSDKDG
60 70 80 90 100
ENSTFDKELV DAEVIITTPF HPGYLTAERL AKAKNLKLAV TAGIGSDHVD
110 120 130 140 150
LDAANKTNGG ITVAEVTGSN VVSVAEHVVM TILLLVRNFV PAHDQIRNGD
160 170 180 190 200
WNVAAVAKNE FDLENKVVGT VGVGRIGERV LRRLKPFDCK ELLYYDYQPL
210 220 230 240 250
RPEVEKEIGA RRVDSLEEMV SQCDVVTINC PLHEKTRGLF NKELISKMKP
260 270 280 290 300
GSWLVNTARG AIVVKEDVAE ALKSGHLRGY GGDVWFPQPA PKEHPLRYAE
310 320 330 340 350
HPWGGGNATV PHMSGTSIDA QIRYANGTKA ILDSYFSGRF DYQPQDLIVH
360
GGDYATKAYG QREKK
Length:365
Mass (Da):40,131
Last modified:November 16, 2011 - v3
Checksum:iC9AB2B4EFBFC540D
GO

Sequence cautioni

The sequence CAA77687.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence EAA57865.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11612 Genomic DNA. Translation: CAA77687.1. Sequence problems.
AACD01000109 Genomic DNA. Translation: EAA57865.1. Sequence problems.
BN001301 Genomic DNA. Translation: CBF70916.1.
PIRiS30088.
RefSeqiXP_664129.1. XM_659037.1.

Genome annotation databases

EnsemblFungiiCADANIAT00007297; CADANIAP00007297; CADANIAG00007297.
GeneIDi2870218.
KEGGiani:AN6525.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11612 Genomic DNA. Translation: CAA77687.1. Sequence problems.
AACD01000109 Genomic DNA. Translation: EAA57865.1. Sequence problems.
BN001301 Genomic DNA. Translation: CBF70916.1.
PIRiS30088.
RefSeqiXP_664129.1. XM_659037.1.

3D structure databases

ProteinModelPortaliQ03134.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi162425.CADANIAP00007297.

Proteomic databases

PRIDEiQ03134.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00007297; CADANIAP00007297; CADANIAG00007297.
GeneIDi2870218.
KEGGiani:AN6525.2.

Phylogenomic databases

eggNOGiCOG1052.
HOGENOMiHOG000136703.
InParanoidiQ03134.
KOiK00122.
OMAiGCRRVEN.
OrthoDBiEOG769ZV3.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiIPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR029753. D-isomer_DH_CS.
IPR029752. D-isomer_DH_CS1.
IPR006140. D-isomer_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view]
PROSITEiPS00065. D_2_HYDROXYACID_DH_1. 1 hit.
PS00670. D_2_HYDROXYACID_DH_2. 1 hit.
PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of the amdA-regulated aciA gene of Aspergillus nidulans."
    Saleeba J.A., Cobbett C.S., Hynes M.J.
    Mol. Gen. Genet. 235:349-358(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  3. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
    Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
    , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
    Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Entry informationi

Entry nameiFDH_EMENI
AccessioniPrimary (citable) accession number: Q03134
Secondary accession number(s): C8V0K7, Q5AYV5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: November 16, 2011
Last modified: January 7, 2015
This is version 98 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.